Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes

Kozak, Marilyn

doi:10.1016/0092-8674(86)90762-2

Cited by 4,741RNA and protein synthesis mechanismsRNA Research and SplicingGenomics and Chromatin Dynamics

Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes

Kozak, Marilyn·1986·Cell

DOI 10.1016/0092-8674(86)90762-2

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Abstract

By analyzing the effects of single base substitutions around the ATG initiator codon in a cloned preproinsulin gene, I have identified ACCATGG as the optimal sequence for initiation by eukaryotic ribosomes. Mutations within that sequence modulate the yield of proinsulin over a 20-fold range. A purine in position -3 (i.e., 3 nucleotides upstream from the ATG codon) has a dominant effect; when a pyrimidine replaces the purine in position -3, translation becomes more sensitive to changes in positions -1, -2, and +4. Single base substitutions around an upstream, out-of-frame ATG codon affect the efficiency with which it acts as a barrier to initiating at the downstream start site for preproinsulin. The optimal sequence for initiation defined by mutagenesis is identical to the consensus sequence that emerged previously from surveys of translational start sites in eukaryotic mRNAs. The mechanism by which nucleotides flanking the ATG codon might exert their effect is discussed.

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The analysis recapitulated the importance of a purine (A or G) at position −3 relative to AUG and a G at +4.
“This analysis recapitulated the importance of a purine (A or G) at position −3 relative to AUG and a G at +4 (Fig. 1e)10,23,24.”
From Human 5′ UTR design and variant effect prediction from a massively parallel translation assay (2019) · cites this paper as [24]
The start codon should include a Kozak sequence.
“The start codon should include Kozak sequence (Kozak 1986), and the stop codon's sequence can be modified (Liu 2005).”
From Modifications of mRNA vaccine structural elements for improving mRNA stability and translation efficiency (2022) · cites this paper as Kozak 1986

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Authors: Kozak, M.
Affiliations: University of Pittsburgh (US)
Corresponding author: Kozak, Marilyn
Venue: Cell
Publisher: Elsevier BV
Published: 1986-01
Volume: 44
Issue: 2
Pages: 283-292
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(86)90762-2
OpenAlex: W2154128645
Cited by: 4,741
References: 0
Citations by year: 2026: 61 · 2025: 49 · 2024: 54 · 2023: 48 · 2022: 60 · 2021: 57 · 2020: 76 · 2019: 56 · 2018: 60 · 2017: 58 · 2016: 49 · 2015: 62 · 2014: 64 · 2013: 50 · 2012: 52
FWCI: 104.73
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM 33915)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: translation initiation, initiator codon, ribosome binding site, translation initiation sites, 80S ribosome
MeSH terms: Animals, Base Sequence, Binding Sites, Chlorocebus aethiops, Cloning, Molecular, Eukaryotic Cells, Hydrogen Bonding, Insulin, Mutation, Nucleic Acid Conformation, Peptide Chain Initiation, Translational, Proinsulin, Protein Precursors, Ribosomes, RNA, Messenger, RNA, Ribosomal

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Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes

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